ID A0A0T2KTY8_9MICO Unreviewed; 540 AA.
AC A0A0T2KTY8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN ORFNames=ASD65_00990 {ECO:0000313|EMBL:KRA23152.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA23152.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA23152.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA23152.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA23152.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA23152.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRA23152.1}.
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DR EMBL; LMGU01000001; KRA23152.1; -; Genomic_DNA.
DR RefSeq; WP_056217220.1; NZ_LMGU01000001.1.
DR AlphaFoldDB; A0A0T2KTY8; -.
DR STRING; 1736570.ASD65_00990; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000051216; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612};
KW Reference proteome {ECO:0000313|Proteomes:UP000051216}.
SQ SEQUENCE 540 AA; 56488 MW; 3A7901CB7D4A809E CRC64;
MSFDIRVTGH VKHVVDETLP GLIADLVASG ITAGDASLWG PAAEAEASKR LGWVQAVTVS
RPLVPEILAL RTELVAKDIT RVVLAGMGGS SLAPEVIAQT AGVPLVILDS TAPGQVLAAL
DGDAESGGLE RTVLVVSSKS GSTVETDSAK RAFEAAFRDL GIDPLERIVV VTDPGSPLDQ
AARADGYRVF NADPTVGGRY SALTAFGLVP TGLAGVDIDE LLTEAEASLL EVAIDSPSNP
ALVLAAAIAG GNPRRDKLGL ITDGTHIIGL PNWIEQLVAE STGKNGTGIL PVVLLPVSPE
VEGKPADLQI VRLVDEAHQF HLFEHHEGEI LISGSLGGQL VVWEYATAIA GRMLGIDPFD
QPDVESAKIA TRGLLDARPE PTAPAFSVEG VEVRVSDPEL AASGTIAGVL DALWARIPAD
GYVSVQAYVN RLELSQLQGL REMVAADSGR PTTFGWGPRF LHSTGQYHKG GPANGVFLQI
LERTDVDLEI PDRPFTFGQL IEAQAAGDAS VLADGHGRPV VTLTLTDPQL EVLALFEAAQ
//
